MECHANISM OF MACROPHAGE RECOGNITION OF SH-OXIDIZED ERYTHROCYTES - RECOGNITION OF GLYCOPHORIN-A ON ERYTHROCYTES BY A MACROPHAGE RECEPTOR FOR SIALOSACCHARIDES

Mouse erythrocytes treated with diamide, an SH-oxidizing agent, attact to mouse resident peritoneal macrophages in the absence of serum. The mechanism by which macrophages recognize the SH-oxidized erythrocytes was investigated. Although phosphatidylserine-liposomes inhibited the macrophage recognition, there was no detectable phosphatidylserine on the outer surface of diamide-treated erythrocytes. It is unlikely that phosphatidylserine, that has been proposed to be a determinant in the recognition of some pathologic erythrocytes by macrophages, is involved in the recognition of diamide-treated erythrocytes. Sialyl lactose and glycophorin A effectively inhibited the macrophage recognition, while lactose and neuraminidase-treated glycophorin A did not. Disialoganglioside G(Dla), but not monosialoganglioside G(M1), partially inhibited the recognition. Trypsinized erythrocytes, in which majority of glycophorin A glycopeptides were expected to be removed from the cell surface, poorly attached to macrophages after diamide treatment. Therefore, it is likely that an interaction between glycophorin A on diamide-treated erythrocytes and a macrophage receptor for sialosaccharides is involved in the recognition. Similar inhibition specificity was observed in the macrophage recognition of erythrocytes treated with periodate, an oxidant that induces disulfide-dependent erythrocyte changes causing macrophage recognition, and of erythrocytes treated with SH-blocking agents, N-ethylmaleimide and p-chloromercuribenzoic acid, that were also found to be susceptible to macrophage recognition in the absence of serum. These results suggest that the macrophages recognize sialosaccharide chains of glycophorin A molecules on SH-oxidized or SH-blocked erythrocytes through a receptor for sialosaccharides.